STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
ftrFormylmethanofuran: tetrahydromethanopterin formyltransferase (Ftr); Catalyzes the reversible transfer of a formyl group from formylmethanofuran (formyl-MFR) to tetrahydromethanopterin (H(4)MPT) so as to produce 5-formyl tetrahydromethanopterin (5-formyl-H(4)MPT) and methanofuran (MFR); Belongs to the FTR family. (302 aa)    
Predicted Functional Partners:
fwdA
Tungsten containing formylmethanofuran dehydrogenase, subunit A; Citation: FEBS Lett. 1989 253: 226-30; Eur. J. Biochem. 1996 242: 156-162.
 
 0.998
mch
N5,N10-methenyltetrahydromethanopterin cyclohydrolase; Catalyzes the reversible interconversion of 5-formyl-H(4)MPT to methenyl-H(4)MPT(+); Belongs to the MCH family.
 
 
 0.997
fwdB
Tungsten containing formylmethanofuran dehydrogenase subunit B; Catalyzes the reversible oxidation of CO(2) and methanofuran (MFR) to N-formylmethanofuran (CHO-MFR). This enzyme is oxygen-labile.
 
 0.997
fmdA
Formylmethanofuran dehydrogenase, subunit A; Citation: FEBS Lett. 1989 253:226-30; Eur. J. Biochem. 1996 242: 156-162.
 
 
 0.996
fmdB
Molybdenum containing formylmethanofuran dehydrogenase, subunit B; Contains selenocysteine; Citation: FEBS Lett. 1989 253:226-30; Eur. J. Biochem. 1996 242:156-162.
 
 
 0.994
fmdB-2
Molybdenum containing formylmethanofuran dehydrogenase, subunit B; Citation: FEBS Lett. 1989 253:226-30; Eur. J. Biochem. 1996 242:156-162.
 
 
 0.994
fwdD
Tungsten containing formylmethanofuran dehydrogenase, subunit D; Citation: Arch. Microbiol. 1998 170: 389-93; FEBS Lett. 1989 253: 226-30; Eur. J. Biochem. 1996 242: 156-162.
 
 
 0.977
fwdC
Tungsten containing formylmethanofuran dehydrogenase, subunit C; Catalyzes the reversible oxidation of CO(2) and methanofuran (MFR) to N-formylmethanofuran (CHO-MFR). This enzyme is oxygen-labile. Belongs to the FwdC/FmdC family.
 
 
 0.977
fmdC
Molybdenum containing formylmethanofuran dehydrogenase subunit C; Citation: FEBS Lett. 1989 253:226-30; Eur. J. Biochem. 1996 242: 156-162.
 
  
 0.976
MMP0070
Tungsten containing formylmethanofruran dehydrogenase subunit C-related protein.
 
  
 0.966
Your Current Organism:
Methanococcus maripaludis S2
NCBI taxonomy Id: 267377
Other names: M. maripaludis S2, Methanococcus maripaludis LL, Methanococcus maripaludis str. S2, Methanococcus maripaludis strain S2
Server load: medium (56%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.